Publication: Detergent-labile, supramolecular assemblies of KcsA: relative abundance and interactions involved
Authors
Giudici Besseghini, Ana Marcela ; Molina Gallego, María Luisa ; Ayala Torres, José Leonardo ; Montoya Díaz, Estefanía ; Renart Pérez, María Lourdes ; Fernández Carvajal, Asia María ; Encinar Hidalgo, José Antonio ; Ferrer Montiel, Antonio Vicente ; Poveda Larrosa, José Antonio ; González Ros, José Manuel
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Publisher
Elsevier
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DOI
https://doi.org/10.1016/j.bbamem.2012.09.020
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info:eu-repo/semantics/article
Description
© 2012 Elsevier B.V. All rights reserved. This document is the Published version of a Published Work that appeared in final form in Biochimica et Biophysica Acta (BBA) - Bioenergetics. To access the final edited and published work see https://doi.org/10.1016/j.bbamem.2012.09.020
Abstract
In this work, we illustrate the ability of the prokaryotic potassium channel KcsA to assemble into a variety of supramolecular clusters of defined sizes containing the tetrameric KcsA as the repeating unit. Such clusters, particularly the larger ones, are markedly detergent-labile and thus, disassemble readily upon exposure to the detergents commonly used in protein purification or conventional electrophoresis analysis. This is a reversible process, as cluster re-assembly occurs upon detergent removal and without the need of added membrane lipids. Interestingly, the dimeric ensemble between two tetrameric KcsA molecules are quite resistant to detergent disassembly to individual KcsA tetramers and along with the latter, are likely the basic building blocks through which the larger clusters are organized. As to the proteins domains involved in clustering, we have observed disassembly of KcsA clusters by SDS-like alkyl sulfates. As these amphiphiles bind to inter-subunit, “non-annular” sites on the protein, these observations suggest that such sites also mediate channel–channel interactions leading to cluster assembly.
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Citation
Biochimica et Biophysica Acta 1828 (2013) 193–200
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